CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity
Highly active CALB cross-linked enzyme aggregates (CLEAs) were synthesized using a layered methodology based on the synthesis of a cross-linked protein cofeeder core over which an external layer of lipase was later cross-linked. The layered CALB CLEAs were characterized in terms of their catalytic a...
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ftconicet:oai:ri.conicet.gov.ar:11336/6549 2023-10-09T21:44:45+02:00 CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity Guauque Torres, María del Pilar Foresti, María Laura Ferreira, Maria Lujan application/pdf http://hdl.handle.net/11336/6549 eng eng Elsevier info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1369703X14001193 info:eu-repo/semantics/altIdentifier/doi/ info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bej.2014.05.004 http://hdl.handle.net/11336/6549 Guauque Torres, María del Pilar; Foresti, María Laura; Ferreira, Maria Lujan; CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity; Elsevier; Biochemical Engineering Journal; 90; 5-2014; 36-43 1369-703X info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ Lipase Immobilization Cleas Cofeeder Core https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.bej.2014.05.004 2023-09-24T19:59:52Z Highly active CALB cross-linked enzyme aggregates (CLEAs) were synthesized using a layered methodology based on the synthesis of a cross-linked protein cofeeder core over which an external layer of lipase was later cross-linked. The layered CALB CLEAs were characterized in terms of their catalytic activity in three different test reactions: esterification of oleic acid and ethanol in absence of solvents, esterification of oleic acid and heptanol in organic medium, and hydrolysis of triolein in emulsioned medium. The impact of the cross-linker/protein mass ratio on CLEAs activity, and its evolution with storage time were evaluated in the solventless synthesis of ethyloleate. The amount of cross-linker used showed to be a key parameter for the evolution of the catalytic activity of CLEAs during storage. Under the best conditions found, hyperactivated CALB CLEAs with up to 188% of recovered activity in ethyl oleate synthesis were obtained. In terms of hydrolytic activity mature layered CALB CLEAs showed a retained activity of 68%. The assay of dried mature layered CALB CLEAs in heptyl oleate synthesis showed catalytic activities much higher than the one exhibited by free CALB, reaching 1 h-fatty acid conversions of 14% and 2%, respectively. The high catalytic activity shown by layered CALB CLEAs, suggests that they are an interesting alternative specially for the catalysis of fatty acid esterifications in both organic and solventless medium. Fil: Guauque Torres, María del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Tecnologia En Polimeros y Nanotecnologia; Argentina Fil: Ferreira, Maria Lujan. ... Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Ferreira ENVELOPE(-62.050,-62.050,-64.600,-64.600) Biochemical Engineering Journal 90 36 43 |
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Open Polar |
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CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
op_collection_id |
ftconicet |
language |
English |
topic |
Lipase Immobilization Cleas Cofeeder Core https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 |
spellingShingle |
Lipase Immobilization Cleas Cofeeder Core https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 Guauque Torres, María del Pilar Foresti, María Laura Ferreira, Maria Lujan CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity |
topic_facet |
Lipase Immobilization Cleas Cofeeder Core https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 |
description |
Highly active CALB cross-linked enzyme aggregates (CLEAs) were synthesized using a layered methodology based on the synthesis of a cross-linked protein cofeeder core over which an external layer of lipase was later cross-linked. The layered CALB CLEAs were characterized in terms of their catalytic activity in three different test reactions: esterification of oleic acid and ethanol in absence of solvents, esterification of oleic acid and heptanol in organic medium, and hydrolysis of triolein in emulsioned medium. The impact of the cross-linker/protein mass ratio on CLEAs activity, and its evolution with storage time were evaluated in the solventless synthesis of ethyloleate. The amount of cross-linker used showed to be a key parameter for the evolution of the catalytic activity of CLEAs during storage. Under the best conditions found, hyperactivated CALB CLEAs with up to 188% of recovered activity in ethyl oleate synthesis were obtained. In terms of hydrolytic activity mature layered CALB CLEAs showed a retained activity of 68%. The assay of dried mature layered CALB CLEAs in heptyl oleate synthesis showed catalytic activities much higher than the one exhibited by free CALB, reaching 1 h-fatty acid conversions of 14% and 2%, respectively. The high catalytic activity shown by layered CALB CLEAs, suggests that they are an interesting alternative specially for the catalysis of fatty acid esterifications in both organic and solventless medium. Fil: Guauque Torres, María del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Tecnologia En Polimeros y Nanotecnologia; Argentina Fil: Ferreira, Maria Lujan. ... |
format |
Article in Journal/Newspaper |
author |
Guauque Torres, María del Pilar Foresti, María Laura Ferreira, Maria Lujan |
author_facet |
Guauque Torres, María del Pilar Foresti, María Laura Ferreira, Maria Lujan |
author_sort |
Guauque Torres, María del Pilar |
title |
CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity |
title_short |
CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity |
title_full |
CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity |
title_fullStr |
CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity |
title_full_unstemmed |
CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity |
title_sort |
cleas of candida antarctica lipase b (calb) with a bovine serum albumin (bsa) cofeeder core. study of their catalytic activity |
publisher |
Elsevier |
url |
http://hdl.handle.net/11336/6549 |
long_lat |
ENVELOPE(-62.050,-62.050,-64.600,-64.600) |
geographic |
Argentina Ferreira |
geographic_facet |
Argentina Ferreira |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1369703X14001193 info:eu-repo/semantics/altIdentifier/doi/ info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bej.2014.05.004 http://hdl.handle.net/11336/6549 Guauque Torres, María del Pilar; Foresti, María Laura; Ferreira, Maria Lujan; CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity; Elsevier; Biochemical Engineering Journal; 90; 5-2014; 36-43 1369-703X |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
op_doi |
https://doi.org/10.1016/j.bej.2014.05.004 |
container_title |
Biochemical Engineering Journal |
container_volume |
90 |
container_start_page |
36 |
op_container_end_page |
43 |
_version_ |
1779313416871084032 |